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. 1970 Oct;46(4):592–595. doi: 10.1104/pp.46.4.592

Nucleoside Diphosphate-Sugar 4-Epimerases

II. Uridine Diphosphate Arabinose 4-Epimerase of Wheat Germ 1

Der-Fong Fan a,2, David Sidney Feingold a,3
PMCID: PMC396641  PMID: 5483919

Abstract

Uridine diphosphate (UDP)-arabinose 4-epimerase (EC 5.1.3.5) has been purified at least 20-fold from wheat germ by MnCl2 treatment, (NH4)2SO4 fractionation, dialysis, and Sephadex and diethylaminoethyl cellulose column chromatography. The enzyme has no action on UDP-d-glucose, UDP-d-glucuronic acid, or TDP-d-glucose. The pH optimum is 8.0. Km values are 1.5 mM for UDP-d-xylose and 0.5 mm for UDP-l-arabinose. The equilibrium constant, K, for the reaction UDP-l-arabinose ⇆ UDP-d-xylose is 1.25. The enzyme is neither activated by nicotinamide adenine dinucleotide nor inhibited by reduced nicotinamide adenine dinucleotide. It is completely inhibited by p-chloromercuri-phenylsulfonate; the inhibition is reversed by cysteine.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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